Mutational analysis of domain II beta of bacteriophage Mu transposase: domains II alpha and II beta belong to different catalytic complementation groups.
This study examines the contribution of domain II beta of bacteriophage Mu transposase (A protein), a subdomain of the central catalytic domain II, to the transposition reaction. The properties of several point mutations implicate a role for this domain in facilitating metal-assisted assembly of the synaptic complex, as well as in intramolecular DNA strand transfer. Point mutations as well as deletions in domain II beta can be complemented by those in domain II alpha but not those in domain III alpha. Thus, residues within subdomains II alpha and II beta belong to different catalytic complementation groups.
Namgoong
S Y
SY
Department of Microbiology, University of Texas at Austin 78712, USA.
Kim
K
K
Saxena
P
P
Yang
J Y
JY
Jayaram
M
M
Giedroc
D P
DP
Harshey
R M
RM
D010583:Bacteriophage mu / Q000201:enzymology*; D001665:Binding Sites; D002384:Catalysis; D005816:Genetic Complementation Test; D007700:Kinetics; D046911:Macromolecular Substances; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017384:Sequence Deletion; D019895:Transposases / Q000737:chemistry* / Q000378:metabolism*; D015032:Zinc / Q000494:pharmacology
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D019895:Transposases; D015032:Zinc